• BMB Reports
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• v.39 no.5
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• pp.530-536
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• 2006

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from $25^{\circ}C$ to $55^{\circ}C$ induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. $42^{\circ}C$. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at $45^{\circ}C$ and $35^{\circ}C$ reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at $45^{\circ}C$ compared to $35^{\circ}C$, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.

• Current Applied Physics
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• v.18 no.11
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• pp.1196-1200
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• 2018

We have experimentally demonstrated circular polarization generation from linear polarized soft X-ray at synchrotron by adopting a thin magnetic film polarizer. Polarizer is composed of Co/Pt multilayer with a perpendicular magnetic anisotropy, which allows us to easily accommodate without needing any tilting angle into the measurement setup since the circular polarization is generated for the X-ray with normal incidence and transmission. Generated circular polarization is examined by observing magnetic domain features based on the X-ray magnetic circular dichroism, where~11% of circular component is estimated compared to the case of full circular polarization.

• Proceedings of the Korean Magnestics Society Conference
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• 2007.05a
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• pp.194.1-194.1
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• 2007

• Journal of Photoscience
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• v.8 no.1
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• pp.39-41
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• 2001

No Abstract. See Full-text

• Bulletin of the Korean Chemical Society
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• v.29 no.9
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• pp.1823-1826
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• 2008

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2000.01a
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• pp.28-28
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• 2000

• Bulletin of the Korean Chemical Society
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• v.6 no.3
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• pp.123-124
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• 1985

The optical activity of a fluid in the extreme critical region, where the Ornstein-Zernike theory does not hold, is explicitly obtained. We suggest new experimental methods to measure the critical exponent for correlation function by using the results of circular dichroism and optical rotation given in this paper.

• Bulletin of the Korean Chemical Society
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• v.11 no.3
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• pp.254-255
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• 1990

• Journal of Photoscience
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• v.11 no.1
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• pp.29-33
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• 2004

The mechanism of interaction of cyanocobalamin (CB) with bovine serum albumin (BSA) has been investigated by spectrofluorometric and circular dichroism methods. Association constant for the CB-BSA system showed that the interaction is non-covalent in nature. Binding studies in the presence of an hydrophobic probe, 8-anilino-l-naphthalene sulphonic acid, sodium salt (ANS) showed that there is hydrophobic interaction between CB and ANS and they do not share common sites in BSA. Stern-Volmer analysis of fluorescence quenching data showed that the fraction of fluorophore (protein) accessible to the quencher (CB) was close to unity indicating thereby that both tryptophan residues of BSA are involved in drug-protein interaction. The rate constant for quenching, greater than $10^{10}$ $M^{-1}$ $s^{-1}$, indicated that the drug binding site is in close proximity to tryptophan residue of BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of CB to BSA involves hydrophobic bonds predominantly. Significant increase in concentration of free drug was observed for CB in presence of paracetamol. Circular dichroism studies revealed the change in helicity of BSA due to binding of CB to BSA.

• BMB Reports
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• v.32 no.6
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• pp.521-528
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• 1999

The folding of recombinant hepatitis B virus X-protein (rHBx) solubilized from Escherichia coli inclusion bodies was investigated. By sequential dialysis of urea, rHBx was folded into its native structure, which was demonstrated by the efficacy of its transcriptional activation of the adenovirus major late promoter (MLP), fluorescence spectroscopy, and circular dichroism (CD) analysis. The decrease in CD values at 220 nm and a corresponding blue shift of the intrinsic fluorescence emission confirmed the ability of rHBx to refold in lower concentrations of urea, yielding the active protein. Equilibrium and kinetic studies of the refolding of rHBx were carried out by tryptophan fluorescence measurements. From the biphasic nature of the fluorescence curves, the existence of stable intermediate states in the renaturation process was inferred. Reverse phase-high performance liquid chromatography (RP-HPLC) analysis further demonstrated the existence of these intermediates and their apparent compactness.